Recombinant Rat L-Selectin/CD62L Fc Chimera Protein, CF

Recombinant Rat L-Selectin/CD62L Fc Chimera Protein, CF Summary

Product Specifications

Product Datasheets

Carrier Free

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Background: L-Selectin/CD62L

L-Selectin (also known as Leukocyte Selectin, LAM-1, LECAM-1, LECCAM-1, TQ1, Leu-8, MEL-14 antigen, DREG, lymph node homing receptor, CD62L) is a member of the Selectin family of cell surface molecules which include E-Selectin and P-Selectin. All Selectins have an extracellular domain composed of an amino-terminal calcium-dependent lectin domain, an epidermal growth factor (EGF)-like domain, two to nine short consensus repeat (SCR) units, a transmembrane domain, and a cytoplasmic tail. L-Selectin expression is limited to hematopoietic cells, with most leukocytes expressing L-Selectin at some stage of differentiation. The majority of myeloid cells, B cells, and virgin T cells express L-Selectin, while only a sub-population of memory T cells and NK cells express L-Selectin. Lymphocytes and neutrophils exhibit a reversible loss of L-Selectin after cellular activation that results from endoproteolytic release of the extracellular portion of receptor from the cell surface. Cleavage of L-Selectin from the cell surface results in a high circulating level of functionally active soluble L-Selectin. All selectins bind sialytated and fucosylated oligosaccharides that are linked to glycoproteins and glycolipids. L-Selectin specifically binds to at least three different heavily glycosolylated mucin-like proteins: GlyCAM-1, CD34, and MAdCAM-1. Multiple studies indicated that L-Selectin, P-Selectin E-Selectin collaborate to mediate the initial binding of leukocytes to endothelium at sites of tissue injury and inflammation, producing the characteristic “rolling” of leukocytes along the endothelium. L-Selectin knockout mice have a 70% decrease in rolling leukocytes in exposed mesentery and have impaired neutrophil and monocyte migration into areas of inflammation. Additionally, L-Selectin knockout mice have relatively few lymphocytes present in peripheral lymph nodes and Peyer’s patches. Short-term in vivo homing experiments in L-Selectin deficient mice demonstrate that L-Selectin is involved in lymphocyte homing to Peyer’s patches and mesenteric lymph nodes in the gut. Rat and human L-Selectin share 77% amino acid sequence homology. Rat and mouse L-Selection share 83% amino acid sequence homology (1, 2).

Related Research Areas

• Adhesion Molecules in Angiogenesis
• B Cell Chemotaxis, Migration, and Adhesion
• Granulocyte Markers
• Lectins
• Lymphoma
• Monocyte Markers
• Mouse Tissue-Resident Macrophage Markers
• Myeloid Lineage Markers
• Myeloid-derived Suppressor Cells (MDSC)
• Natural Killer T (NKT) Cells
• Neutrophils
• Regulatory T Cells (Tregs)
• Selectins
• T Cell Migration/Adhesion